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Biochemical and structural characterisation of a protozoan beta-carbonic anhydrase from Trichomonas vaginalis.
J Enzyme Inhib Med Chem. 2020 Dec; 35(1):1292-1299.JE

Abstract

We report the biochemical and structural characterisation of a beta-carbonic anhydrase (β-CA) from Trichomonas vaginalis, a unicellular parasite responsible for one of the world's leading sexually transmitted infections, trichomoniasis. CAs are ubiquitous metalloenzymes belonging to eight evolutionarily divergent groups (α, β, γ, δ, ζ, η, θ, and ι); humans express only α-CAs, whereas many clinically significant pathogens express only β- and/or γ-CAs. For this reason, the latter two groups of CAs are promising biomedical targets for novel antiinfective agents. The β-CA from T. vaginalis (TvaCA1) was recombinantly produced and biochemically characterised. The crystal structure was determined, revealing the canonical dimeric fold of β-CAs and the main features of the enzyme active site. The comparison with the active site of human CA enzymes revealed significant differences that can be exploited for the design of inhibitors selective for the protozoan enzyme with respect to the human ones.

Authors+Show Affiliations

Faculty of Medicine and Health Technology, Tampere University, Tampere, Finland.Institute of Biostructures and Bioimaging of the National Research Council, Naples, Italy.Faculty of Medicine and Health Technology, Tampere University, Tampere, Finland.Faculty of Medicine and Health Technology, Tampere University, Tampere, Finland. Fimlab Ltd, Tampere, Finland.Faculty of Medicine and Health Technology, Tampere University, Tampere, Finland.Institute of Biostructures and Bioimaging of the National Research Council, Naples, Italy.Institute of Biostructures and Bioimaging of the National Research Council, Naples, Italy.Neurofarba Department, Sezione di Chimica Farmaceutica e Nutraceutica, Università degli Studi di Firenze, Sesto Fiorentino, Italy.Department of Energy and Environmental Biotechnology, National Institute of Genetic Engineering and Biotechnology, (NIGEB), Tehran, Iran.Neurofarba Department, Sezione di Chimica Farmaceutica e Nutraceutica, Università degli Studi di Firenze, Sesto Fiorentino, Italy.Institute of Biostructures and Bioimaging of the National Research Council, Naples, Italy.Faculty of Medicine and Health Technology, Tampere University, Tampere, Finland. Fimlab Ltd, Tampere, Finland.

Pub Type(s)

Journal Article

Language

eng

PubMed ID

32515610

Citation

Urbański, Linda J., et al. "Biochemical and Structural Characterisation of a Protozoan Beta-carbonic Anhydrase From Trichomonas Vaginalis." Journal of Enzyme Inhibition and Medicinal Chemistry, vol. 35, no. 1, 2020, pp. 1292-1299.
Urbański LJ, Di Fiore A, Azizi L, et al. Biochemical and structural characterisation of a protozoan beta-carbonic anhydrase from Trichomonas vaginalis. J Enzyme Inhib Med Chem. 2020;35(1):1292-1299.
Urbański, L. J., Di Fiore, A., Azizi, L., Hytönen, V. P., Kuuslahti, M., Buonanno, M., Monti, S. M., Angeli, A., Zolfaghari Emameh, R., Supuran, C. T., De Simone, G., & Parkkila, S. (2020). Biochemical and structural characterisation of a protozoan beta-carbonic anhydrase from Trichomonas vaginalis. Journal of Enzyme Inhibition and Medicinal Chemistry, 35(1), 1292-1299. https://doi.org/10.1080/14756366.2020.1774572
Urbański LJ, et al. Biochemical and Structural Characterisation of a Protozoan Beta-carbonic Anhydrase From Trichomonas Vaginalis. J Enzyme Inhib Med Chem. 2020;35(1):1292-1299. PubMed PMID: 32515610.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Biochemical and structural characterisation of a protozoan beta-carbonic anhydrase from Trichomonas vaginalis. AU - Urbański,Linda J, AU - Di Fiore,Anna, AU - Azizi,Latifeh, AU - Hytönen,Vesa P, AU - Kuuslahti,Marianne, AU - Buonanno,Martina, AU - Monti,Simona M, AU - Angeli,Andrea, AU - Zolfaghari Emameh,Reza, AU - Supuran,Claudiu T, AU - De Simone,Giuseppina, AU - Parkkila,Seppo, PY - 2020/6/10/entrez PY - 2020/6/10/pubmed PY - 2020/6/10/medline KW - Beta carbonic anhydrase KW - Trichomonas vaginalis KW - crystal structure KW - kinetics KW - protozoan SP - 1292 EP - 1299 JF - Journal of enzyme inhibition and medicinal chemistry JO - J Enzyme Inhib Med Chem VL - 35 IS - 1 N2 - We report the biochemical and structural characterisation of a beta-carbonic anhydrase (β-CA) from Trichomonas vaginalis, a unicellular parasite responsible for one of the world's leading sexually transmitted infections, trichomoniasis. CAs are ubiquitous metalloenzymes belonging to eight evolutionarily divergent groups (α, β, γ, δ, ζ, η, θ, and ι); humans express only α-CAs, whereas many clinically significant pathogens express only β- and/or γ-CAs. For this reason, the latter two groups of CAs are promising biomedical targets for novel antiinfective agents. The β-CA from T. vaginalis (TvaCA1) was recombinantly produced and biochemically characterised. The crystal structure was determined, revealing the canonical dimeric fold of β-CAs and the main features of the enzyme active site. The comparison with the active site of human CA enzymes revealed significant differences that can be exploited for the design of inhibitors selective for the protozoan enzyme with respect to the human ones. SN - 1475-6374 UR - https://www.unboundmedicine.com/medline/citation/32515610/Biochemical_and_structural_characterisation_of_a_protozoan_beta-carbonic_anhydrase_from_Trichomonas_vaginalis L2 - http://www.tandfonline.com/doi/full/10.1080/14756366.2020.1774572 DB - PRIME DP - Unbound Medicine ER -
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